Addgene: pExp-MBP
AB Vector - pAB-MBP™
Magnetic nanoparticles for the affinity adsorption of maltose binding protein (MBP) fusion enzymes - Journal of Materials Chemistry (RSC Publishing)
Maltose-Binding Protein (MBP), a Secretion-Enhancing Tag for Mammalian Protein Expression Systems | PLOS ONE
Magnetic nanoparticles for the affinity adsorption of maltose binding protein (MBP) fusion enzymes - Journal of Materials Chemistry (RSC Publishing) DOI:10.1039/C2JM16778F
MBP-Trap Agarose beads, kit | Proteintech
Recombinant Protein: E. coli-Based Expression - BioProcess InternationalBioProcess International
One-step affinity purification of fusion proteins with optimal monodispersity and biological activity: application to aggregation-prone HPV E6 proteins | Microbial Cell Factories | Full Text
Purified human mini-calpain-5 is well folded (A) The maltose binding... | Download Scientific Diagram
A designed fusion tag for soluble expression and selective separation of extracellular domains of fibroblast growth factor receptors | Scientific Reports
Addgene: pKK-MBP-TEV
Maltose-binding protein - Wikipedia
IJMS | Free Full-Text | Soluble Cytoplasmic Expression and Purification of Immunotoxin HER2(scFv)-PE24B as a Maltose Binding Protein Fusion
Anti-MBP-Tag | Mouse Maltose Binding Protein-Tag Antibody | Cell Applications
Frontiers | A Novel and Fast Purification Method for Nucleoside Transporters
Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter | PNAS
Improving Recombinant Protein Solubility Using the MBP Tag
Recombinant purification definition - BiologicsCorp
Tagged Protein Purification | Cytiva
Passenger sequences can promote interlaced dimers in a common variant of the maltose-binding protein | Scientific Reports
Improving Recombinant Protein Solubility Using the MBP Tag
Amylose (MBP-tag affinity) Magnetic Beads - Advanced BioChemicals
Maltose Binding Protein (MBP) Control Protein (000-001-385-1) | Rockland
Frontiers | Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system
